HAMAP rule MF_00117
General rule information
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Accession |
MF_00117 |
Dates |
1-JUN-2001 (Created) 18-NOV-2019 (Last updated, Version 20) |
Propagated annotation
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Identifier, protein and gene names
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Protein name |
RecName:
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Full=33 kDa chaperonin;
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AltName:
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Full=Heat shock protein 33 homolog;
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Short=HSP33;
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Function |
Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. |
Subcellular location |
Cytoplasm. |
Ptm |
Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive. |
Similarity |
Belongs to the HSP33 family. |
GO:0051082; Molecular function: unfolded protein binding.
GO:0005737; Cellular component: cytoplasm.
From: HSLO_ECOLI (P0A6Y5) |
Key
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From
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To
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Description
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Tag
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Condition
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FTGroup
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DISULFID
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230
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232
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Redox-active
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C-x-C
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DISULFID
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263
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266
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Redox-active
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C-x(2)-C
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Additional information
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Size range |
281-341 amino acids |
Related rules |
None |
Fusion |
None |
Comments |
Possible wrong start in AQUAE and DEIRA |